NCBI Conserved Domain Search

Conserved domains on [gi|1515654337|gb|ROP25966|]

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methenyltetrahydrofolate cyclohydrolase /5,10-methylenetetrahydrofolate dehydrogenase (NADP+) [Vibrio crassostreae]

Protein Classification

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase( domain architecture ID 11484949)

bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/ 5,10-methenyltetrahydrofolate cyclohydrolase reversibly catalyzes oxidation of 5,10-methylene-THF to 5,10-methenyl-THF and hydrolysis of 5,10-methenyl-THF to 10-formyl-THF

CATH: 3.40.50.720|3.40.50.10860

EC: 1.5.1.5|3.5.4.9

Gene Ontology: GO:0004488|GO:0003824|GO:0016787|GO:0009086|GO:0006164|GO:0006730

PubMed: 1748668|10386884

SCOP: 4000102

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PRK10792

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-285

0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 598.44 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK10792    1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK10792   81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:PRK10792  161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFHSK 285
Cdd:PRK10792  241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285

Name

Accession

Description

Interval

E-value

PRK10792

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-285

0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 598.44 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK10792    1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK10792   81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:PRK10792  161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFHSK 285
Cdd:PRK10792  241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285

FolD

COG0190

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...

1-283

0e+00

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 518.80 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGlRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:COG0190     1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:COG0190    80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:COG0190   160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFH 283
Cdd:COG0190   240 VGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282

THF_DHG_CYH_C

pfam02882

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

124-283

1.65e-96

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

Pssm-ID: 427036 Cd Length: 160 Bit Score: 280.51 E-value: 1.65e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 124 HPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 204 DVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFH 283
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160

NAD_bind_m-THF_DH_Cyclohyd

cd01080

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...

116-280

1.15e-92

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.

Pssm-ID: 133448 Cd Length: 168 Bit Score: 271.35 E-value: 1.15e-92

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 116 PEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKD 195
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 196 LEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLE---SGKLVGDVEYDVAKESASFITPVPGGVGPMTVASLI 272
Cdd:cd01080    81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPdksGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160


                  ....*...
gi 1515654337 273 ENTMIACE 280
Cdd:cd01080   161 KNTVEAAK 168

Name

Accession

Description

Interval

E-value

PRK10792

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-285

0e+00

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 598.44 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK10792    1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK10792   81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:PRK10792  161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFHSK 285
Cdd:PRK10792  241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285

FolD

COG0190

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...

1-283

0e+00

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 518.80 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGlRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:COG0190     1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:COG0190    80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:COG0190   160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFH 283
Cdd:COG0190   240 VGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282

PRK14189

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

1-281

3.04e-142

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 401.37 E-value: 3.04e-142

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLRaPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14189    1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK14189   80 ARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:PRK14189  160 HAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGKL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQ 281
Cdd:PRK14189  240 CGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280

PRK14190

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-285

4.67e-138

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 390.53 E-value: 4.67e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLrAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14190    1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGI-VPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK14190   80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:PRK14190  160 HVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFHSK 285
Cdd:PRK14190  240 CGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284

PRK14188

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

2-279

1.26e-127

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 364.66 E-value: 1.26e-127

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   2 TAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLT 81
Cdd:PRK14188    1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  82 LVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKH 161
Cdd:PRK14188   81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 162 AVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLES---- 237
Cdd:PRK14188  161 AVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPApekg 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1515654337 238 ---GKLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIAC 279
Cdd:PRK14188  241 egkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAA 285

PRK14184

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-278

2.34e-124

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 356.01 E-value: 2.34e-124

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14184    4 LDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVV 165
Cdd:PRK14184   84 LNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVVV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 166 GASNIVGRPMTLELLLAG----CTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGkLV 241
Cdd:PRK14184  164 GRSNIVGKPLALMLGAPGkfanATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG-LV 242

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1515654337 242 GDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIA 278
Cdd:PRK14184  243 GDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279

PRK14191

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

4-280

5.10e-124

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 355.23 E-value: 5.10e-124

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   4 QNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLV 83
Cdd:PRK14191    2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  84 DQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAV 163
Cdd:PRK14191   82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVGD 243
Cdd:PRK14191  162 IIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVGD 241

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1515654337 244 VEYDVAKESASFITPVPGGVGPMTVASLIENTMIACE 280
Cdd:PRK14191  242 VDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278

PRK14186

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

2-283

1.45e-118

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 341.66 E-value: 1.45e-118

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   2 TAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLT 81
Cdd:PRK14186    1 MALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  82 LVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKH 161
Cdd:PRK14186   81 LIAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 162 AVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLES---- 237
Cdd:PRK14186  161 AVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSsdgk 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1515654337 238 GKLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIA-CEQFH 283
Cdd:PRK14186  241 TRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSwQKRHG 287

PRK14183

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

4-282

2.39e-113

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 327.94 E-value: 2.39e-113

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   4 QNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLV 83
Cdd:PRK14183    2 QILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  84 DQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAV 163
Cdd:PRK14183   82 AMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVGD 243
Cdd:PRK14183  162 VVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLVGD 241

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1515654337 244 VEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQF 282
Cdd:PRK14183  242 VDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNR 280

PRK14193

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-281

6.55e-112

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 324.27 E-value: 6.55e-112

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGlRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14193    1 MTAIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK14193   80 AVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAG--CTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESG 238
Cdd:PRK14193  160 HVVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDG 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1515654337 239 KLVGDVEYDVAkESASFITPVPGGVGPMTVASLIENTMIACEQ 281
Cdd:PRK14193  240 KLVGDVHPDVW-EVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281

PRK14179

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

3-279

4.32e-108

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 314.77 E-value: 4.32e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   3 AQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTL 82
Cdd:PRK14179    2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  83 VDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHA 162
Cdd:PRK14179   82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVG 242
Cdd:PRK14179  162 VVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKLIG 241

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1515654337 243 DVEYDVAKESASFITPVPGGVGPMTVASLIENTMIAC 279
Cdd:PRK14179  242 DVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAA 278

PRK14174

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-283

8.85e-108

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 314.45 E-value: 8.85e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14174    4 IDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIED 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAqrMPKLR----SCTPKGIITLLDRYNIDLRGKH 161
Cdd:PRK14174   84 LNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLV--MGHLDkcfvSCTPYGILELLGRYNIETKGKH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 162 AVVVGASNIVGRPMTlELLL-----AGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLE 236
Cdd:PRK14174  162 CVVVGRSNIVGKPMA-NLMLqklkeSNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1515654337 237 -----SG-KLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFH 283
Cdd:PRK14174  241 dpstkSGyRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERVN 293

PRK14166

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-276

1.49e-106

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 310.80 E-value: 1.49e-106

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLRaPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14166    4 LDGKALSAKIKEELKEKNQFLKSKGIE-SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPK-LRSCTPKGIITLLDRYNIDLRGKHAVV 164
Cdd:PRK14166   83 LNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAVI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVGDV 244
Cdd:PRK14166  163 IGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGDV 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1515654337 245 EYDVAKESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PRK14166  243 DFEEVSKKSSYITPVPGGVGPMTIAMLLENTV 274

PRK14176

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-281

1.18e-101

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 298.64 E-value: 1.18e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKA-RTEAGLrAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVD 84
Cdd:PRK14176   11 IDGKALAKKIEAEVRSGVERlKSNRGI-TPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  85 QLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVV 164
Cdd:PRK14176   90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRlESGKLVGDV 244
Cdd:PRK14176  170 VGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITK-EEDKVYGDV 248

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1515654337 245 EYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQ 281
Cdd:PRK14176  249 DFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285

PRK14194

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-283

1.18e-101

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 299.07 E-value: 1.18e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLRaPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14194    2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK14194   81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESG-- 238
Cdd:PRK14194  161 HAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDgr 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1515654337 239 -KLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFH 283
Cdd:PRK14194  241 sRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQA 286

PRK14182

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-276

1.75e-101

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 298.09 E-value: 1.75e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLrAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14182    4 IDGKQIAAKVKGEVATEVRALAARGV-QTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKL-RSCTPKGIITLLDRYNIDLRGKHAVV 164
Cdd:PRK14182   83 LNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRALV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVGDV 244
Cdd:PRK14182  163 VGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVGDV 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1515654337 245 EYDVAKESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PRK14182  243 EFAAAAARASAITPVPGGVGPMTRAMLLVNTV 274

PRK14178

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-278

1.31e-100

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 295.60 E-value: 1.31e-100

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTvRSEVaarVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14178    3 LDGKAVSEK-RLEL---LKEEIIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVV 165
Cdd:PRK14178   79 LNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 166 GASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLEsGKLVGDVE 245
Cdd:PRK14178  159 GRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVN-GKLCGDVD 237

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1515654337 246 YDVAKESASFITPVPGGVGPMTVASLIENTMIA 278
Cdd:PRK14178  238 FDAVKEIAGAITPVPGGVGPMTIATLMENTFDA 270

PLN02616

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

3-284

3.22e-100

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 297.69 E-value: 3.22e-100

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   3 AQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTL 82
Cdd:PLN02616   73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  83 VDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQ--RMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PLN02616  153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrgREPLFVPCTPKGCIELLHRYNVEIKGK 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESG-- 238
Cdd:PLN02616  233 RAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDAss 312

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1515654337 239 ----KLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFHS 284
Cdd:PLN02616  313 prgyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRIHN 362

PRK14167

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

3-278

1.25e-99

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 293.61 E-value: 1.25e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   3 AQNIDGKLISQTVRSEVAARVKARTEAGLRaPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTL 82
Cdd:PRK14167    2 TEIIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  83 VDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHA 162
Cdd:PRK14167   81 IDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 163 VVVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESG 238
Cdd:PRK14167  161 VVVGRSDIVGKPMANLLIQKAdggnATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAD 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1515654337 239 -----KLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIA 278
Cdd:PRK14167  241 tekgyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKA 285

PLN02516

methylenetetrahydrofolate dehydrogenase (NADP+)

2-276

2.35e-99

methylenetetrahydrofolate dehydrogenase (NADP+)

Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 293.34 E-value: 2.35e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   2 TAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLT 81
Cdd:PLN02516    8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  82 LVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQ--RMPKLRSCTPKGIITLLDRYNIDLRG 159
Cdd:PLN02516   88 KVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMkgREPLFLPCTPKGCLELLSRSGIPIKG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 160 KHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRL---- 235
Cdd:PLN02516  168 KKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVsdps 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1515654337 236 -ESG-KLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PLN02516  248 kKSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTV 290

PRK14180

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-283

1.15e-98

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 290.78 E-value: 1.15e-98

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14180    4 IDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPK-LRSCTPKGIITLLDRYNIDLRGKHAVV 164
Cdd:PRK14180   84 LNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKcLESCTPKGIMTMLREYGIKTEGAYAVV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLEsGKLVGDV 244
Cdd:PRK14180  164 VGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVD-GKIVGDV 242

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1515654337 245 EYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFH 283
Cdd:PRK14180  243 DFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELN 281

PRK14185

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

4-278

1.80e-98

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 290.58 E-value: 1.80e-98

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   4 QNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLV 83
Cdd:PRK14185    2 QLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  84 DQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAV 163
Cdd:PRK14185   82 RELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 164 VVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESG- 238
Cdd:PRK14185  162 VLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDAt 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1515654337 239 -----KLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIA 278
Cdd:PRK14185  242 rksgfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLA 286

PRK14169

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-283

4.98e-97

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 286.84 E-value: 4.98e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   3 AQNIDGKLISQTVRSEVAARVKARTEAGLrAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTL 82
Cdd:PRK14169    1 ATRLDGRAVSKKILADLKQTVAKLAQQDV-TPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  83 VDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHA 162
Cdd:PRK14169   80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVG 242
Cdd:PRK14169  160 VIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLLG 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1515654337 243 DVEYDVAKESASFITPVPGGVGPMTVASLIENTM-IACEQFH 283
Cdd:PRK14169  240 DVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVtLAKRRAN 281

THF_DHG_CYH_C

pfam02882

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

124-283

1.65e-96

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

Pssm-ID: 427036 Cd Length: 160 Bit Score: 280.51 E-value: 1.65e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 124 HPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQA 203
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 204 DVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQFH 283
Cdd:pfam02882  81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160

PRK14192

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-281

8.98e-96

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 283.66 E-value: 8.98e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14192    1 MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK14192   81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKl 240
Cdd:PRK14192  161 HAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGG- 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQ 281
Cdd:PRK14192  240 VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK 280

PLN02897

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

2-276

3.39e-95

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 284.16 E-value: 3.39e-95

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   2 TAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLT 81
Cdd:PLN02897   55 KTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  82 LVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQ--RMPKLRSCTPKGIITLLDRYNIDLRG 159
Cdd:PLN02897  135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 160 KHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESG- 238
Cdd:PLN02897  215 KNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSs 294

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1515654337 239 -----KLVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PLN02897  295 cefgyRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTL 337

PRK14173

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-280

8.69e-95

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 280.95 E-value: 8.69e-95

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAglraPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14173    1 MAARELSGPPAAEAVYAELRARLAKLPFV----PHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK14173   77 ELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRL--ESG 238
Cdd:PRK14173  157 EVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVggNGG 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1515654337 239 K--LVGDVEYDVAkESASFITPVPGGVGPMTVASLIENTMIACE 280
Cdd:PRK14173  237 RdiLTGDVHPEVA-EVAGALTPVPGGVGPMTVAMLMANTVIAAL 279

PRK14175

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-278

4.28e-93

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 276.80 E-value: 4.28e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLrAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14175    1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGF-TPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGK 160
Cdd:PRK14175   80 NELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 161 HAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKL 240
Cdd:PRK14175  160 NAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKL 239

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMIA 278
Cdd:PRK14175  240 KGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLA 277

NAD_bind_m-THF_DH_Cyclohyd

cd01080

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...

116-280

1.15e-92

Pssm-ID: 133448 Cd Length: 168 Bit Score: 271.35 E-value: 1.15e-92

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 116 PEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKD 195
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 196 LEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLE---SGKLVGDVEYDVAKESASFITPVPGGVGPMTVASLI 272
Cdd:cd01080    81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPdksGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160


                  ....*...
gi 1515654337 273 ENTMIACE 280
Cdd:cd01080   161 KNTVEAAK 168

PRK14177

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-285

2.80e-92

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 274.54 E-value: 2.80e-92

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14177    6 LDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVV 165
Cdd:PRK14177   86 LNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 166 GASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINrleSGKlVGDVE 245
Cdd:PRK14177  166 GRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN---PGN-VGDIE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1515654337 246 YDVAKESASFITPVPGGVGPMTVASLIENTMI-ACEQFHSK 285
Cdd:PRK14177  242 ISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYsFKEHFTPP 282

PRK14187

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-281

2.68e-91

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 272.47 E-value: 2.68e-91

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14187    5 IDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRL--AQRMPKLRSCTPKGIITLLDRYNIDLRGKHAV 163
Cdd:PRK14187   85 LNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLftGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESG---KL 240
Cdd:PRK14187  165 VIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGgvkKF 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1515654337 241 VGDVEYDVAKESASFITPVPGGVGPMTVASLIENTMI-ACEQ 281
Cdd:PRK14187  245 VGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIaACNQ 286

PRK14172

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

4-282

1.24e-87

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 262.41 E-value: 1.24e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   4 QNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLV 83
Cdd:PRK14172    3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  84 DQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAV 163
Cdd:PRK14172   83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 164 VVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLEsGKLVGD 243
Cdd:PRK14172  163 VIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVN-GKITGD 241

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1515654337 244 VEYDVAKESASFITPVPGGVGPMTVASLIENtmiACEQF 282
Cdd:PRK14172  242 VNFDKVIDKASYITPVPGGVGSLTTTLLIKN---VCEAL 277

PRK14171

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-278

2.73e-83

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 251.80 E-value: 2.73e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:PRK14171    5 IDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPK-LRSCTPKGIITLLDRYNIDLRGKHAVV 164
Cdd:PRK14171   85 LNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQgFIPCTALGCLAVIKKYEPNLTGKNVVI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 165 VGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVGDV 244
Cdd:PRK14171  165 IGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKIIGDV 244

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1515654337 245 EYDVAKESASFITPVPGGVGPMTVASLIENTMIA 278
Cdd:PRK14171  245 DFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278

PRK14168

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-276

7.32e-82

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 248.64 E-value: 7.32e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   1 MTAQNIDGKLISQTVRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELL 80
Cdd:PRK14168    1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  81 TLVDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRL--AQRMPKLRSCTPKGIITLLDRYNIDLR 158
Cdd:PRK14168   81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLmiGGDEVKFLPCTPAGIQEMLVRSGVETS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 159 GKHAVVVGASNIVGRPMTLELLLAG----CTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINR 234
Cdd:PRK14168  161 GAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1515654337 235 L----ESGK--LVGDVEYDVAKESASFITPVPGGVGPMTVASLIENTM 276
Cdd:PRK14168  241 VgtneSTGKaiLSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTL 288

PRK14181

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

15-275

3.31e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 246.70 E-value: 3.31e-81

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  15 VRSEVAARVKARTEAGLRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQLNQDPEIDG 94
Cdd:PRK14181    8 AAEHILATIKENISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  95 ILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGR-LAQRMPKLRSCTPKGIITLLDRYNIDLRGKHAVVVGASNIVGR 173
Cdd:PRK14181   88 ILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKlLLGETDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 174 PMTLELLL----AGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGK-----LVGDV 244
Cdd:PRK14181  168 PLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANpkgyiLVGDV 247

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1515654337 245 EYDVAKESASFITPVPGGVGPMTVASLIENT 275
Cdd:PRK14181  248 DFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278

PRK14170

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-281

2.88e-79

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 241.52 E-value: 2.88e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   3 AQNIDGKLISQTVRSEVAARVKARTEAGlRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTL 82
Cdd:PRK14170    2 GEIIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337  83 VDQLNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVDGFHPYNVGRLAQRMPKLRSCTPKGIITLLDRYNIDLRGKHA 162
Cdd:PRK14170   81 VEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 163 VVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKPNFIPGAWIKKGAVVVDVGINRLESGKLVG 242
Cdd:PRK14170  161 VVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCG 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1515654337 243 DVEYDVAKESASFITPVPGGVGPMTVASLIENTMIACEQ 281
Cdd:PRK14170  241 DVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279

THF_DHG_CYH

pfam00763

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

6-121

2.29e-62

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 192.23 E-value: 2.29e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337   6 IDGKLISQTVRSEVAARVKARTEAGlRAPGLAVVLVGEDPASQVYVGSKRKACEEVGFVSKSYDLPATATEDELLTLVDQ 85
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1515654337  86 LNQDPEIDGILVQLPLPAGIDSTHVLERITPEKDVD 121
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115

NAD_bind_m-THF_DH_Cyclohyd_like

cd05212

NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...

141-280

2.07e-33

NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.

Pssm-ID: 133451 Cd Length: 140 Bit Score: 119.15 E-value: 2.07e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 141 CTPKGI-------ITLLDRYNIDLRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHRFTKDLEGHVRQADVVVVAVGKP 213
Cdd:cd05212     3 CTPLFVspvakavKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSPKP 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1515654337 214 NFIPGAWIKKGAVVVDVGINRLesgklvgdvEYDVAKESASFITPVPGGVGPMTVASLIENTMIACE 280
Cdd:cd05212    83 EKVPTEWIKPGATVINCSPTKL---------SGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140

NAD_bind_m-THF_DH

cd01079

NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...

116-274

1.02e-10

NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.

Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 59.75 E-value: 1.02e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 116 PEKDVDGFHPYNVGRL--------AQRMPK-LRSCTPKGIITLLD---------RYNIDLRGKHAVVVGASNIVGRPMTL 177
Cdd:cd01079     1 PHKDVEGLSHKYIFNLyhnirfldPENRKKsILPCTPLAIVKILEflgiynkilPYGNRLYGKTITIINRSEVVGRPLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 178 ELLLAGCTT---------------------TTCHRFTKDLEGHVRQADVVVVAVGKPNF-IPGAWIKKGAVVVDV-GINR 234
Cdd:cd01079    81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFaSIKN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1515654337 235 LEsgklvgdveyDVAKESASFITPVpggVGPMTVASLIEN 274
Cdd:cd01079   161 FE----------PSVKEKASIYVPS---IGKVTIAMLLRN 187

COG5322

Predicted amino acid dehydrogenase [General function prediction only];

150-231

1.50e-03

Predicted amino acid dehydrogenase [General function prediction only];

Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 39.44 E-value: 1.50e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515654337 150 LDRYNIDLRGKHAVVVGASNIVGRPMTLELLLAGCTTTTCHR---------------------FTKDLEGHVRQADVVVV 208
Cdd:COG5322   142 AERMGIDLKKATVAVVGATGSIGSVCARLLAREVKRLTLVARnlerleelaeeilrnpggkvtITTDIDEALREADIVVT 221

                          90       100
                  ....*....|....*....|....*
gi 1515654337 209 AVGKPNFI--PGAwIKKGAVVVDVG 231
Cdd:COG5322   222 VTSAVGAIidPED-LKPGAVVCDVA 245

L-AlaDH

cd05305

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...

193-232

7.21e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.

Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 37.38 E-value: 7.21e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1515654337 193 TKDLEGHVRQADVVVVAVgkpnFIPGA------------WIKKGAVVVDVGI 232
Cdd:cd05305   222 PANLEEALKEADLVIGAV----LIPGAkapklvteemvkTMKPGSVIVDVAI 269

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01